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PredicateObject
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http://www.biopax.org/relea...
http://www.biopax.org/relea...
Cathepsin B
http://www.biopax.org/relea...
CATB_HUMAN
http://www.biopax.org/relea...
http://www.biopax.org/relea...
3.4.22.1, APP secretase, APPS, Cathepsin B heavy chain, Cathepsin B light chain, Cathepsin B1
http://www.biopax.org/relea...
FUNCTION: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis. CATALYTIC ACTIVITY: Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides. SUBUNIT: Dimer of a heavy chain and a light chain cross-linked by a disulfide bond. Interacts with SRPX2. SUBCELLULAR LOCATION: Lysosome. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. SIMILARITY: Belongs to the peptidase C1 family. WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/CTSBID40202ch8p23.html"; GENE SYNONYMS: CPSB. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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